Myosin light chain kinase A is activated by cGMP-dependent and cGMP-independent pathways.
FEBS Lett
; 580(8): 2059-64, 2006 Apr 03.
Article
em En
| MEDLINE
| ID: mdl-16546177
ABSTRACT
Stimulation of Dictyostelium cells with the chemoattractant cAMP results in transient phosphorylation of the myosin regulatory light chain (RLC). We show that myosin light chain kinase A (MLCK-A) is responsible for RLC phosphorylation during chemotaxis, and that MLCK-A itself is transiently phosphorylated on threonine-166, dramatically increasing its catalytic activity. MLCK-A activation during chemotaxis is highly responsive to cellular cGMP levels and the cGMP-binding protein GbpC. MLCK-A- cells have a partial cytokinesis defect, and do not phosphorylate RLC in response to concanavalin A (conA), but cells lacking cGMP or GbpC divide normally and phosphorylate in response to conA. Thus MLCK-A is activated by a cGMP/GbpC-independent mechanism activated during cytokinesis or by conA, and a cGMP/GbpC-dependent pathway during chemotaxis.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Quinase de Cadeia Leve de Miosina
/
GMP Cíclico
Limite:
Animals
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2006
Tipo de documento:
Article
País de afiliação:
Estados Unidos